HEADER TRANSFERASE/TRANSFERASE INHIBITOR 24-OCT-12 4HPU
TITLE CRYSTAL STRUCTURE OF THE CATALYTIC SUBUNIT OF CAMP-DEPENDENT PROTEIN
TITLE 2 KINASE DISPLAYING PARTIAL PHOSPHORYL TRANSFER OF AMP-PNP ONTO A
TITLE 3 SUBSTRATE PEPTIDE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: CAMP-DEPENDENT PROTEIN KINASE CATALYTIC SUBUNIT ALPHA;
COMPND 3 CHAIN: E;
COMPND 4 SYNONYM: PKA C-ALPHA;
COMPND 5 EC: 2.7.11.11;
COMPND 6 ENGINEERED: YES;
COMPND 7 MOL_ID: 2;
COMPND 8 MOLECULE: CAMP-DEPENDENT PROTEIN KINASE INHIBITOR ALPHA;
COMPND 9 CHAIN: I;
COMPND 10 FRAGMENT: SP20 PEPTIDE DERIVED FROM CAMP-DEPENDENT PROTEIN KINASE
COMPND 11 INHIBITOR ALPHA (UNP RESIDUES 6-25);
COMPND 12 SYNONYM: PKI-ALPHA, CAMP-DEPENDENT PROTEIN KINASE INHIBITOR,
COMPND 13 MUSCLE/BRAIN ISOFORM;
COMPND 14 ENGINEERED: YES;
COMPND 15 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: MUS MUSCULUS;
SOURCE 3 ORGANISM_COMMON: MOUSE;
SOURCE 4 ORGANISM_TAXID: 10090;
SOURCE 5 GENE: PRKACA, PKACA;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 MOL_ID: 2;
SOURCE 9 SYNTHETIC: YES;
SOURCE 10 ORGANISM_SCIENTIFIC: MUS MUSCULUS;
SOURCE 11 ORGANISM_COMMON: MOUSE;
SOURCE 12 ORGANISM_TAXID: 10090;
SOURCE 13 OTHER_DETAILS: SYNTHETIC PEPTIDE
KEYWDS PROTEIN KINASE FOLD, PHOSPHOTRANSFERASE, REGULATORY SUBUNITS, PKI,
KEYWDS 2 MAGNESIUM, PHOSPHORYLATION, TRANSFERASE-TRANSFERASE INHIBITOR
KEYWDS 3 COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR A.C.BASTIDAS,J.M.STEICHEN,J.WU,S.S.TAYLOR
REVDAT 5 15-NOV-17 4HPU 1 REMARK
REVDAT 4 10-APR-13 4HPU 1 JRNL
REVDAT 3 03-APR-13 4HPU 1 REMARK
REVDAT 2 27-MAR-13 4HPU 1 JRNL
REVDAT 1 20-MAR-13 4HPU 0
JRNL AUTH A.C.BASTIDAS,M.S.DEAL,J.M.STEICHEN,Y.GUO,J.WU,S.S.TAYLOR
JRNL TITL PHOSPHORYL TRANSFER BY PROTEIN KINASE A IS CAPTURED IN A
JRNL TITL 2 CRYSTAL LATTICE.
JRNL REF J.AM.CHEM.SOC. V. 135 4788 2013
JRNL REFN ISSN 0002-7863
JRNL PMID 23458248
JRNL DOI 10.1021/JA312237Q
REMARK 2
REMARK 2 RESOLUTION. 1.55 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.5.0110
REMARK 3 AUTHORS : MURSHUDOV,VAGIN,DODSON
REMARK 3
REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.55
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 61.91
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.5
REMARK 3 NUMBER OF REFLECTIONS : 62785
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : THROUGHOUT
REMARK 3 FREE R VALUE TEST SET SELECTION : RANDOM
REMARK 3 R VALUE (WORKING + TEST SET) : 0.173
REMARK 3 R VALUE (WORKING SET) : 0.172
REMARK 3 FREE R VALUE : 0.194
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100
REMARK 3 FREE R VALUE TEST SET COUNT : 3357
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 20
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 1.55
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.59
REMARK 3 REFLECTION IN BIN (WORKING SET) : 4566
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 98.87
REMARK 3 BIN R VALUE (WORKING SET) : 0.2460
REMARK 3 BIN FREE R VALUE SET COUNT : 248
REMARK 3 BIN FREE R VALUE : 0.2580
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 2936
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 70
REMARK 3 SOLVENT ATOMS : 432
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 15.15
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.57000
REMARK 3 B22 (A**2) : -0.53000
REMARK 3 B33 (A**2) : -0.03000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 0.00000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.072
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.072
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.042
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 2.523
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.961
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.949
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 3138 ; 0.009 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 4266 ; 1.329 ; 1.985
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 378 ; 5.394 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 151 ;35.373 ;23.974
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 552 ;13.293 ;15.082
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 18 ;17.404 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 450 ; 0.090 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 2349 ; 0.006 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) OTHERS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 MAIN-CHAIN BOND REFINED ATOMS (A**2): 1815 ; 0.666 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 2937 ; 1.253 ; 2.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 1323 ; 1.860 ; 3.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 1319 ; 3.011 ; 4.500
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ANISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 RIGID-BOND RESTRAINTS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; FREE ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; BONDED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 NCS RESTRAINTS STATISTICS
REMARK 3 NUMBER OF DIFFERENT NCS GROUPS : NULL
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 5
REMARK 3
REMARK 3 TLS GROUP : 1
REMARK 3 NUMBER OF COMPONENTS GROUP : 3
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : E 12 E 350
REMARK 3 RESIDUE RANGE : E 402 E 402
REMARK 3 RESIDUE RANGE : I 600 I 600
REMARK 3 ORIGIN FOR THE GROUP (A): -9.0944 13.3922 -20.9222
REMARK 3 T TENSOR
REMARK 3 T11: 0.0112 T22: 0.0083
REMARK 3 T33: 0.0164 T12: -0.0022
REMARK 3 T13: -0.0002 T23: 0.0023
REMARK 3 L TENSOR
REMARK 3 L11: 0.0608 L22: 0.2169
REMARK 3 L33: 0.4220 L12: -0.0185
REMARK 3 L13: -0.0482 L23: 0.1696
REMARK 3 S TENSOR
REMARK 3 S11: -0.0140 S12: -0.0095 S13: -0.0136
REMARK 3 S21: -0.0270 S22: 0.0002 S23: 0.0304
REMARK 3 S31: -0.0139 S32: 0.0076 S33: 0.0138
REMARK 3
REMARK 3 TLS GROUP : 2
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : I 5 I 23
REMARK 3 ORIGIN FOR THE GROUP (A): 3.8220 1.3754 -26.3031
REMARK 3 T TENSOR
REMARK 3 T11: 0.0214 T22: 0.0170
REMARK 3 T33: 0.0176 T12: 0.0129
REMARK 3 T13: 0.0008 T23: -0.0029
REMARK 3 L TENSOR
REMARK 3 L11: 0.3179 L22: 1.9079
REMARK 3 L33: 1.4195 L12: -0.7723
REMARK 3 L13: -0.5888 L23: 1.2815
REMARK 3 S TENSOR
REMARK 3 S11: -0.0156 S12: -0.0234 S13: 0.0277
REMARK 3 S21: 0.0139 S22: 0.0328 S23: -0.0912
REMARK 3 S31: 0.0516 S32: 0.0328 S33: -0.0173
REMARK 3
REMARK 3 TLS GROUP : 3
REMARK 3 NUMBER OF COMPONENTS GROUP : 2
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : E 501 E 882
REMARK 3 RESIDUE RANGE : I 701 I 750
REMARK 3 ORIGIN FOR THE GROUP (A): -7.5788 12.4899 -19.0227
REMARK 3 T TENSOR
REMARK 3 T11: 0.0037 T22: 0.0103
REMARK 3 T33: 0.0115 T12: 0.0016
REMARK 3 T13: 0.0016 T23: 0.0002
REMARK 3 L TENSOR
REMARK 3 L11: 0.0935 L22: 0.2012
REMARK 3 L33: 0.5454 L12: -0.0085
REMARK 3 L13: -0.0403 L23: 0.1815
REMARK 3 S TENSOR
REMARK 3 S11: -0.0079 S12: -0.0140 S13: -0.0111
REMARK 3 S21: -0.0237 S22: -0.0103 S23: 0.0178
REMARK 3 S31: -0.0136 S32: 0.0309 S33: 0.0183
REMARK 3
REMARK 3 TLS GROUP : 4
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : E 403 E 403
REMARK 3 ORIGIN FOR THE GROUP (A): -2.5470 13.8146 -15.7667
REMARK 3 T TENSOR
REMARK 3 T11: 0.0131 T22: 0.0374
REMARK 3 T33: 0.0620 T12: 0.0195
REMARK 3 T13: 0.0292 T23: 0.0517
REMARK 3 L TENSOR
REMARK 3 L11: 0.0000 L22: 0.0000
REMARK 3 L33: 0.0000 L12: 0.0000
REMARK 3 L13: 0.0000 L23: 0.0000
REMARK 3 S TENSOR
REMARK 3 S11: 0.0000 S12: 0.0000 S13: 0.0000
REMARK 3 S21: 0.0000 S22: 0.0000 S23: 0.0000
REMARK 3 S31: 0.0000 S32: 0.0000 S33: 0.0000
REMARK 3
REMARK 3 TLS GROUP : 5
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : E 404 E 404
REMARK 3 ORIGIN FOR THE GROUP (A): -3.7320 10.2267 -16.8168
REMARK 3 T TENSOR
REMARK 3 T11: 0.0618 T22: 0.0119
REMARK 3 T33: 0.0145 T12: 0.0108
REMARK 3 T13: 0.0275 T23: 0.0120
REMARK 3 L TENSOR
REMARK 3 L11: 0.0000 L22: 0.0000
REMARK 3 L33: 0.0000 L12: 0.0000
REMARK 3 L13: 0.0000 L23: 0.0000
REMARK 3 S TENSOR
REMARK 3 S11: 0.0000 S12: 0.0000 S13: 0.0000
REMARK 3 S21: 0.0000 S22: 0.0000 S23: 0.0000
REMARK 3 S31: 0.0000 S32: 0.0000 S33: 0.0000
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : MASK
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.40
REMARK 3 ION PROBE RADIUS : 0.80
REMARK 3 SHRINKAGE RADIUS : 0.80
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING
REMARK 3 POSITIONS
REMARK 4
REMARK 4 4HPU COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 31-OCT-12.
REMARK 100 THE DEPOSITION ID IS D_1000075769.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : NULL
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 8.0
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ALS
REMARK 200 BEAMLINE : 8.2.1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : NULL
REMARK 200 WAVELENGTH OR RANGE (A) : 1.0
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315R
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : MOSFLM
REMARK 200 DATA SCALING SOFTWARE : SCALA
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 66294
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.550
REMARK 200 RESOLUTION RANGE LOW (A) : 61.910
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.7
REMARK 200 DATA REDUNDANCY : 5.700
REMARK 200 R MERGE (I) : 0.07600
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 12.8000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.55
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.63
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.2
REMARK 200 DATA REDUNDANCY IN SHELL : 5.70
REMARK 200 R MERGE FOR SHELL (I) : 0.44600
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 3.200
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: NULL
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: MOLECULAR REPLACEMENT
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 53.16
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.63
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 50 MM BICINE, 150 MM AMMONIUM ACETATE,
REMARK 280 10 MM DTT, ~7-10 MG/ML PROTEIN WELL SOLUTION: 2% MPD IN A 1 ML
REMARK 280 WELL. 80 UL OF METHANOL WAS ADDED TO THE WELL IMMEDIATELY BEFORE
REMARK 280 SEALING. DROP WAS 8 UL OF 1:1 PROTEIN:WELL, VAPOR DIFFUSION,
REMARK 280 HANGING DROP, TEMPERATURE 277.15K, PH 8.0
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X+1/2,-Y,Z+1/2
REMARK 290 3555 -X,Y+1/2,-Z+1/2
REMARK 290 4555 X+1/2,-Y+1/2,-Z
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 28.84500
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 49.07000
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 39.90000
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 49.07000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 28.84500
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 39.90000
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: E, I
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465 M RES C SSSEQI
REMARK 465 GLY E 1
REMARK 465 ASN E 2
REMARK 465 ALA E 3
REMARK 465 ALA E 4
REMARK 465 ALA E 5
REMARK 465 ALA E 6
REMARK 465 LYS E 7
REMARK 465 LYS E 8
REMARK 465 GLY E 9
REMARK 465 SER E 10
REMARK 465 GLU E 11
REMARK 465 ASP I 24
REMARK 470
REMARK 470 MISSING ATOM
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 470 I=INSERTION CODE):
REMARK 470 M RES CSSEQI ATOMS
REMARK 470 GLN E 12 CG CD OE1 NE2
REMARK 470 GLU E 13 CG CD OE1 OE2
REMARK 470 SER E 14 OG
REMARK 470 PHE E 318 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 LYS E 319 CG CD CE NZ
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT
REMARK 500
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI DISTANCE
REMARK 500 OE1 GLU E 121 O HOH E 598 1.99
REMARK 500 OG SER E 259 O HOH E 641 2.02
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: TORSION ANGLES
REMARK 500
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)
REMARK 500
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400
REMARK 500
REMARK 500 M RES CSSEQI PSI PHI
REMARK 500 ASP E 166 45.50 -147.24
REMARK 500 ASP E 184 78.80 63.83
REMARK 500
REMARK 500 REMARK: NULL
REMARK 610
REMARK 610 MISSING HETEROATOM
REMARK 610 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 610 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 610 I=INSERTION CODE):
REMARK 610 M RES C SSEQI
REMARK 610 MYR E 401
REMARK 620
REMARK 620 METAL COORDINATION
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG E 404 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ANP I 600 O2G
REMARK 620 2 ANP I 600 O2A 152.5
REMARK 620 3 ANP E 402 O2A 159.9 9.2
REMARK 620 4 HOH E 596 O 94.8 88.1 91.9
REMARK 620 5 ASN E 171 OD1 111.0 96.5 88.6 82.3
REMARK 620 6 ASP E 184 OD2 90.7 89.6 84.8 172.2 90.6
REMARK 620 7 ANP E 402 N3B 81.6 70.9 78.7 97.8 167.3 88.5
REMARK 620 8 HOH I 747 O 24.5 153.3 152.4 115.3 99.2 68.9 92.3
REMARK 620 9 ANP I 600 N3B 67.5 85.1 93.0 96.3 177.9 90.9 14.4 80.0
REMARK 620 N 1 2 3 4 5 6 7 8
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG E 403 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HOH I 714 O
REMARK 620 2 SEP I 21 O1P 106.4
REMARK 620 3 ANP I 600 O1B 99.1 94.3
REMARK 620 4 ANP I 600 O3G 113.1 8.9 87.4
REMARK 620 5 ANP E 402 O1B 93.1 100.0 7.3 93.6
REMARK 620 6 HOH E 595 O 91.6 86.5 168.6 92.1 170.5
REMARK 620 7 ASP E 184 OD2 158.3 94.8 83.9 88.5 87.9 84.7
REMARK 620 8 ASP E 184 OD1 100.5 152.1 88.8 146.3 85.8 85.3 57.9
REMARK 620 N 1 2 3 4 5 6 7
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MYR E 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ANP E 402
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG E 403
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG E 404
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ANP I 600
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR CHAIN I OF CAMP-DEPENDENT
REMARK 800 PROTEIN KINASE INHIBITOR ALPHA
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 4HPT RELATED DB: PDB
REMARK 900 SAME COMPLEX DISPLAYING COMPLETE PHOSPHORYL TRANSFER
DBREF 4HPU E 1 350 UNP P05132 KAPCA_MOUSE 2 351
DBREF 4HPU I 5 24 UNP P63248 IPKA_MOUSE 6 25
SEQADV 4HPU ALA I 20 UNP P63248 ASN 21 ENGINEERED MUTATION
SEQADV 4HPU SEP I 21 UNP P63248 ALA 22 ENGINEERED MUTATION
SEQRES 1 E 350 GLY ASN ALA ALA ALA ALA LYS LYS GLY SER GLU GLN GLU
SEQRES 2 E 350 SER VAL LYS GLU PHE LEU ALA LYS ALA LYS GLU ASP PHE
SEQRES 3 E 350 LEU LYS LYS TRP GLU THR PRO SER GLN ASN THR ALA GLN
SEQRES 4 E 350 LEU ASP GLN PHE ASP ARG ILE LYS THR LEU GLY THR GLY
SEQRES 5 E 350 SER PHE GLY ARG VAL MET LEU VAL LYS HIS LYS GLU SER
SEQRES 6 E 350 GLY ASN HIS TYR ALA MET LYS ILE LEU ASP LYS GLN LYS
SEQRES 7 E 350 VAL VAL LYS LEU LYS GLN ILE GLU HIS THR LEU ASN GLU
SEQRES 8 E 350 LYS ARG ILE LEU GLN ALA VAL ASN PHE PRO PHE LEU VAL
SEQRES 9 E 350 LYS LEU GLU PHE SER PHE LYS ASP ASN SER ASN LEU TYR
SEQRES 10 E 350 MET VAL MET GLU TYR VAL ALA GLY GLY GLU MET PHE SER
SEQRES 11 E 350 HIS LEU ARG ARG ILE GLY ARG PHE SEP GLU PRO HIS ALA
SEQRES 12 E 350 ARG PHE TYR ALA ALA GLN ILE VAL LEU THR PHE GLU TYR
SEQRES 13 E 350 LEU HIS SER LEU ASP LEU ILE TYR ARG ASP LEU LYS PRO
SEQRES 14 E 350 GLU ASN LEU LEU ILE ASP GLN GLN GLY TYR ILE GLN VAL
SEQRES 15 E 350 THR ASP PHE GLY PHE ALA LYS ARG VAL LYS GLY ARG THR
SEQRES 16 E 350 TRP TPO LEU CYS GLY THR PRO GLU TYR LEU ALA PRO GLU
SEQRES 17 E 350 ILE ILE LEU SER LYS GLY TYR ASN LYS ALA VAL ASP TRP
SEQRES 18 E 350 TRP ALA LEU GLY VAL LEU ILE TYR GLU MET ALA ALA GLY
SEQRES 19 E 350 TYR PRO PRO PHE PHE ALA ASP GLN PRO ILE GLN ILE TYR
SEQRES 20 E 350 GLU LYS ILE VAL SER GLY LYS VAL ARG PHE PRO SER HIS
SEQRES 21 E 350 PHE SER SER ASP LEU LYS ASP LEU LEU ARG ASN LEU LEU
SEQRES 22 E 350 GLN VAL ASP LEU THR LYS ARG PHE GLY ASN LEU LYS ASN
SEQRES 23 E 350 GLY VAL ASN ASP ILE LYS ASN HIS LYS TRP PHE ALA THR
SEQRES 24 E 350 THR ASP TRP ILE ALA ILE TYR GLN ARG LYS VAL GLU ALA
SEQRES 25 E 350 PRO PHE ILE PRO LYS PHE LYS GLY PRO GLY ASP THR SER
SEQRES 26 E 350 ASN PHE ASP ASP TYR GLU GLU GLU GLU ILE ARG VAL SEP
SEQRES 27 E 350 ILE ASN GLU LYS CYS GLY LYS GLU PHE THR GLU PHE
SEQRES 1 I 20 THR THR TYR ALA ASP PHE ILE ALA SER GLY ARG THR GLY
SEQRES 2 I 20 ARG ARG ALA SEP ILE HIS ASP
MODRES 4HPU SEP E 139 SER PHOSPHOSERINE
MODRES 4HPU TPO E 197 THR PHOSPHOTHREONINE
MODRES 4HPU SEP E 338 SER PHOSPHOSERINE
MODRES 4HPU SEP I 21 SER PHOSPHOSERINE
HET SEP E 139 10
HET TPO E 197 11
HET SEP E 338 10
HET SEP I 21 10
HET MYR E 401 10
HET ANP E 402 27
HET MG E 403 1
HET MG E 404 1
HET ANP I 600 31
HETNAM SEP PHOSPHOSERINE
HETNAM TPO PHOSPHOTHREONINE
HETNAM MYR MYRISTIC ACID
HETNAM ANP PHOSPHOAMINOPHOSPHONIC ACID-ADENYLATE ESTER
HETNAM MG MAGNESIUM ION
HETSYN SEP PHOSPHONOSERINE
HETSYN TPO PHOSPHONOTHREONINE
FORMUL 1 SEP 3(C3 H8 N O6 P)
FORMUL 1 TPO C4 H10 N O6 P
FORMUL 3 MYR C14 H28 O2
FORMUL 4 ANP 2(C10 H17 N6 O12 P3)
FORMUL 5 MG 2(MG 2+)
FORMUL 8 HOH *432(H2 O)
HELIX 1 1 GLN E 12 THR E 32 1 21
HELIX 2 2 GLN E 39 ASP E 41 5 3
HELIX 3 3 LYS E 76 LEU E 82 1 7
HELIX 4 4 GLN E 84 GLN E 96 1 13
HELIX 5 5 GLU E 127 GLY E 136 1 10
HELIX 6 6 SEP E 139 LEU E 160 1 22
HELIX 7 7 LYS E 168 GLU E 170 5 3
HELIX 8 8 THR E 201 LEU E 205 5 5
HELIX 9 9 ALA E 206 LEU E 211 1 6
HELIX 10 10 LYS E 217 GLY E 234 1 18
HELIX 11 11 GLN E 242 GLY E 253 1 12
HELIX 12 12 SER E 262 LEU E 273 1 12
HELIX 13 13 VAL E 288 ASN E 293 1 6
HELIX 14 14 HIS E 294 ALA E 298 5 5
HELIX 15 15 ASP E 301 GLN E 307 1 7
HELIX 16 16 THR I 6 ALA I 12 1 7
SHEET 1 A 5 PHE E 43 THR E 51 0
SHEET 2 A 5 GLY E 55 HIS E 62 -1 O LEU E 59 N LYS E 47
SHEET 3 A 5 HIS E 68 ASP E 75 -1 O MET E 71 N MET E 58
SHEET 4 A 5 ASN E 115 GLU E 121 -1 O MET E 118 N LYS E 72
SHEET 5 A 5 LEU E 106 LYS E 111 -1 N PHE E 108 O VAL E 119
SHEET 1 B 2 LEU E 162 ILE E 163 0
SHEET 2 B 2 LYS E 189 ARG E 190 -1 O LYS E 189 N ILE E 163
SHEET 1 C 2 LEU E 172 ILE E 174 0
SHEET 2 C 2 ILE E 180 VAL E 182 -1 O GLN E 181 N LEU E 173
LINK C PHE E 138 N SEP E 139 1555 1555 1.33
LINK C SEP E 139 N GLU E 140 1555 1555 1.33
LINK C TRP E 196 N TPO E 197 1555 1555 1.34
LINK C TPO E 197 N LEU E 198 1555 1555 1.33
LINK C VAL E 337 N SEP E 338 1555 1555 1.32
LINK C SEP E 338 N ILE E 339 1555 1555 1.33
LINK C ALA I 20 N SEP I 21 1555 1555 1.32
LINK C SEP I 21 N ILE I 22 1555 1555 1.33
LINK MG MG E 404 O2GBANP I 600 1555 1555 1.77
LINK MG MG E 403 O HOH I 714 1555 1555 1.83
LINK O1P SEP I 21 MG MG E 403 1555 1555 1.96
LINK MG MG E 403 O1BBANP I 600 1555 1555 1.97
LINK MG MG E 404 O2ABANP I 600 1555 1555 2.02
LINK MG MG E 403 O3GBANP I 600 1555 1555 2.11
LINK O2AAANP E 402 MG MG E 404 1555 1555 2.13
LINK MG MG E 404 O HOH E 596 1555 1555 2.14
LINK O1BAANP E 402 MG MG E 403 1555 1555 2.15
LINK MG MG E 403 O HOH E 595 1555 1555 2.15
LINK OD1 ASN E 171 MG MG E 404 1555 1555 2.20
LINK OD2 ASP E 184 MG MG E 404 1555 1555 2.24
LINK OD2 ASP E 184 MG MG E 403 1555 1555 2.26
LINK OD1 ASP E 184 MG MG E 403 1555 1555 2.28
LINK N3BAANP E 402 MG MG E 404 1555 1555 2.33
LINK MG MG E 404 O HOH I 747 1555 1555 2.49
LINK MG MG E 404 N3BBANP I 600 1555 1555 2.55
SITE 1 AC1 2 LEU E 152 GLU E 155
SITE 1 AC2 23 VAL E 57 ALA E 70 LYS E 72 VAL E 104
SITE 2 AC2 23 MET E 120 GLU E 121 TYR E 122 VAL E 123
SITE 3 AC2 23 GLU E 127 GLU E 170 ASN E 171 LEU E 173
SITE 4 AC2 23 THR E 183 ASP E 184 PHE E 327 MG E 403
SITE 5 AC2 23 MG E 404 HOH E 521 HOH E 596 HOH E 740
SITE 6 AC2 23 ARG I 18 SEP I 21 HOH I 714
SITE 1 AC3 6 ASP E 184 ANP E 402 HOH E 595 SEP I 21
SITE 2 AC3 6 ANP I 600 HOH I 714
SITE 1 AC4 6 ASN E 171 ASP E 184 ANP E 402 HOH E 596
SITE 2 AC4 6 ANP I 600 HOH I 747
SITE 1 AC5 31 LEU E 49 GLY E 50 GLY E 52 VAL E 57
SITE 2 AC5 31 ALA E 70 LYS E 72 VAL E 104 MET E 120
SITE 3 AC5 31 GLU E 121 VAL E 123 GLU E 127 LYS E 168
SITE 4 AC5 31 GLU E 170 ASN E 171 LEU E 173 THR E 183
SITE 5 AC5 31 ASP E 184 PHE E 327 MG E 403 MG E 404
SITE 6 AC5 31 HOH E 521 HOH E 595 HOH E 596 ARG I 18
SITE 7 AC5 31 ALA I 20 SEP I 21 HOH I 702 HOH I 714
SITE 8 AC5 31 HOH I 729 HOH I 747 HOH I 750
SITE 1 AC6 77 THR E 51 SER E 53 LEU E 82 GLN E 84
SITE 2 AC6 77 GLU E 86 LEU E 89 ARG E 93 GLU E 127
SITE 3 AC6 77 PHE E 129 ARG E 133 LYS E 168 PRO E 169
SITE 4 AC6 77 GLU E 170 ASP E 184 PHE E 187 LYS E 189
SITE 5 AC6 77 ARG E 190 VAL E 191 LYS E 192 LEU E 198
SITE 6 AC6 77 CYS E 199 GLY E 200 THR E 201 GLU E 203
SITE 7 AC6 77 GLU E 230 TYR E 235 PRO E 236 PHE E 239
SITE 8 AC6 77 ALA E 240 ASP E 241 ILE E 246 TYR E 330
SITE 9 AC6 77 GLU E 349 ANP E 402 MG E 403 HOH E 514
SITE 10 AC6 77 HOH E 518 HOH E 592 HOH E 595 HOH E 728
SITE 11 AC6 77 HOH E 882 ANP I 600 HOH I 701 HOH I 703
SITE 12 AC6 77 HOH I 704 HOH I 705 HOH I 706 HOH I 707
SITE 13 AC6 77 HOH I 708 HOH I 709 HOH I 710 HOH I 711
SITE 14 AC6 77 HOH I 712 HOH I 713 HOH I 714 HOH I 715
SITE 15 AC6 77 HOH I 716 HOH I 717 HOH I 718 HOH I 719
SITE 16 AC6 77 HOH I 720 HOH I 721 HOH I 723 HOH I 726
SITE 17 AC6 77 HOH I 729 HOH I 731 HOH I 732 HOH I 735
SITE 18 AC6 77 HOH I 737 HOH I 740 HOH I 742 HOH I 744
SITE 19 AC6 77 HOH I 746 HOH I 747 HOH I 748 HOH I 749
SITE 20 AC6 77 HOH I 750
CRYST1 57.690 79.800 98.140 90.00 90.00 90.00 P 21 21 21 4
ORIGX1 1.000000 0.000000 0.000000 0.00000
ORIGX2 0.000000 1.000000 0.000000 0.00000
ORIGX3 0.000000 0.000000 1.000000 0.00000
SCALE1 0.017334 0.000000 0.000000 0.00000
SCALE2 0.000000 0.012531 0.000000 0.00000
SCALE3 0.000000 0.000000 0.010190 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
